M
Matthias Altmeyer
Researcher at University of Zurich
Publications - 83
Citations - 6440
Matthias Altmeyer is an academic researcher from University of Zurich. The author has contributed to research in topics: DNA repair & DNA damage. The author has an hindex of 31, co-authored 75 publications receiving 5055 citations. Previous affiliations of Matthias Altmeyer include MESA+ Institute for Nanotechnology & University of Copenhagen.
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Journal ArticleDOI
PARP1 ADP-ribosylates lysine residues of the core histone tails
Simon Messner,Matthias Altmeyer,Hongtao Zhao,Andrea Pozivil,Bernd Roschitzki,Peter Gehrig,Dorothea Rutishauser,Danzhi Huang,Amedeo Caflisch,Michael O. Hottiger +9 more
TL;DR: Computational and experimental results provide strong evidence that PARP1 modifies important regulatory lysines of the core histone tails of all core histones.
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53BP1 fosters fidelity of homology-directed DNA repair
TL;DR: It is shown that when challenged by DSBs, BRCA1- and 53BP1-deficient cells may become hypersensitive to, and be eliminated by, RAD52 inhibition, and it is suggested that such cells survive DSB assaults at the cost of increasing reliance on RAD52-mediated HDR, which may fuel genome instability.
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Readers of poly(ADP-ribose): designed to be fit for purpose
TL;DR: An overview on the current understanding of the writers of this modification and their targets, as well as the enzymes that degrade and thereby modify and erase poly(ADP-ribose) (PAR).
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A short G1 phase imposes constitutive replication stress and fork remodelling in mouse embryonic stem cells.
Akshay K. Ahuja,Karolina Jodkowska,Federico Teloni,Anna H. Bizard,Ralph Zellweger,Raquel Herrador,Sagrario Ortega,Ian D. Hickson,Matthias Altmeyer,Juan Méndez,Massimo Lopes +10 more
TL;DR: It is proposed that rapid cell cycle progression makes ESCs dependent on effective replication-coupled mechanisms to protect genome integrity and H2AX phosphorylation is dependent on Ataxia telangiectasia and Rad3 related (ATR) and is associated with chromatin loading of the ssDNA-binding proteins RPA and RAD51.
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Quantitative analysis of the binding affinity of poly(ADP-ribose) to specific binding proteins as a function of chain length.
TL;DR: It is demonstrated that the affinity of the non-covalent PAR interactions with specific binding proteins (XPA, p53) can be very high (nanomolar range) and depends both on the PAR chain length and on the binding protein.